Abstract

Two recent crystal structures of membrane attack complex/perforin (MACPF) domains found in the complement and perforin families unexpectedly reveal that some proteins of the immune system share a common core fold with their bacterial targets. Although a relationship between MACPF proteins and the previously characterized bacterial cholesterol-dependent cytolysins (CDCs) is not detectable by sequence analysis, the MACPF structures show that eukaryotic defense and bacterial CDC attack share a common mechanism of membrane insertion and pore formation.